The authors thank Mrs. Seiko Oka (Center for Instrumental Analysis, Hokkaido Univ.) for her skillful assistance with mass spectrometry and amino acid analysis.
Isolation of Peptides with Angiotensin I-converting Enzyme Inhibitory Effect Derived from Hydrolysate of Upstream Chum Salmon Muscle
Version of Record online: 20 JUL 2006
Journal of Food Science
Volume 68, Issue 5, pages 1611–1614, June 2003
How to Cite
Ono, S., Hosokawa, M., Miyashita, K. and Takahashi, K. (2003), Isolation of Peptides with Angiotensin I-converting Enzyme Inhibitory Effect Derived from Hydrolysate of Upstream Chum Salmon Muscle. Journal of Food Science, 68: 1611–1614. doi: 10.1111/j.1365-2621.2003.tb12300.x
- Issue online: 20 JUL 2006
- Version of Record online: 20 JUL 2006
- MS 20020089 Submitted 12/6/02, Revised 1/9/03, Accepted 2/21/03, Received 2/26/03
- angiotensin I-converting enzyme inhibitory peptides;
- antihypertensive effect;
- chum salmon;
In order to utilize upstream chum salmon as a component of nutraceutical food, their defatted muscle proteins were hydrolyzed with 5% thermolysin. The resulting hydrolysate showed high inhibitory activity against angiotensin I-converting enzyme (inhibitory concentration50= 27.9 protein μg/mL) in vitro. A significant reduction of systolic blood pressure was observed when 500 and 2000 mg/kg of body weight were orally administered into spontaneously hypertensive rats. Angiotensin I-converting enzyme inhibitory peptides contained in the hydrolysate were isolated with various chromatographs. These 6 active peptides were Trp residue-containing dipeptides: Trp-Ala, Val-Trp, Trp-Met, Met-Trp, Ile-Trp, and Leu-Trp. The inhibitory concentration50 values of these dipeptides ranged from 2.5 μM to 277.3 μM.